2015
CCM2–CCM3 interaction stabilizes their protein expression and permits endothelial network formation
Draheim KM, Li X, Zhang R, Fisher OS, Villari G, Boggon TJ, Calderwood DA. CCM2–CCM3 interaction stabilizes their protein expression and permits endothelial network formation. Journal Of Cell Biology 2015, 208: 987-1001. PMID: 25825518, PMCID: PMC4384732, DOI: 10.1083/jcb.201407129.Peer-Reviewed Original ResearchMeSH KeywordsApoptosis Regulatory ProteinsBinding SitesCarrier ProteinsCell LineCell ProliferationCentral Nervous SystemCrystallography, X-RayGene ExpressionHemangioma, Cavernous, Central Nervous SystemHumansMembrane ProteinsMutagenesisNeovascularization, PhysiologicPaxillinProtein BindingProtein Interaction MappingProtein Structure, TertiaryProteolysisProto-Oncogene ProteinsRNA InterferenceRNA, Small InterferingSequence AlignmentConceptsBinding-deficient mutantStructure-guided mutagenesisNormal cell growthCerebral cavernous malformationsEndothelial network formationHomology domainCCM3 proteinsProteasomal degradationEndothelial cell network formationMolecular basisCell network formationEssential adaptorCell growthFunctional significanceCCM3 expressionX-ray crystallographyProtein expressionCCM2CCM3Network formationExpressionMutantsHP1MutagenesisAdaptor
2014
Cerebral cavernous malformation proteins at a glance
Draheim KM, Fisher OS, Boggon TJ, Calderwood DA. Cerebral cavernous malformation proteins at a glance. Journal Of Cell Science 2014, 127: 701-707. PMID: 24481819, PMCID: PMC3924200, DOI: 10.1242/jcs.138388.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosis Regulatory ProteinsCapillary PermeabilityCarrier ProteinsCentral Nervous System NeoplasmsHemangioma, Cavernous, Central Nervous SystemHumansKRIT1 ProteinMembrane ProteinsMicrotubule-Associated ProteinsNeoplasm ProteinsProto-Oncogene ProteinsRho GTP-Binding ProteinsSignal TransductionConceptsAdaptor proteinCerebral Cavernous Malformation ProteinsMulti-domain adaptor proteinBasic cellular processesProtein-protein interactionsCerebral cavernous malformationsAccompanying posterGlance articleCCM proteinsCellular processesProtein functionCellular phenotypesTrimeric complexFunction mutationsCell adhesionCell scienceProteinLeaky blood vesselsFocal neurological defectsCurrent understandingNeurological defectsCytoskeletalGenesPDCD10KRIT1
2001
PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase
Formstecher E, Ramos J, Fauquet M, Calderwood D, Hsieh J, Canton B, Nguyen X, Barnier J, Camonis J, Ginsberg M, Chneiweiss H. PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase. Developmental Cell 2001, 1: 239-250. PMID: 11702783, DOI: 10.1016/s1534-5807(01)00035-1.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActive Transport, Cell NucleusAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsBlotting, NorthernCell DivisionCell NucleusCell SurvivalCHO CellsCricetinaeCytoplasmDNA, ComplementaryDose-Response Relationship, DrugGreen Fluorescent ProteinsImmunohistochemistryLuminescent ProteinsMAP Kinase Signaling SystemMiceMicroscopy, FluorescenceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesModels, BiologicalMolecular Sequence DataMutationPhosphoproteinsPrecipitin TestsProtein BindingSequence Homology, Amino AcidTime FactorsTranscription, GeneticTransfectionTwo-Hybrid System TechniquesConceptsERK MAP kinasePEA-15MAP kinaseERK nuclear localizationNuclear export sequenceERK-dependent transcriptionMAP kinase pathwayMultiple cell typesERK 1/2 MAP kinase pathwayExport sequenceSubcellular localizationNuclear localizationCytoplasmic sequestrationKinase pathwayIntegrin functionCell typesCell growthKinaseBiological outcomesCell proliferationGenetic deletionTranscriptionERKLocalizationProliferation